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Interaction of spectrin with the low molecular weight phosphotyrosine phosphatase [LMW-PTP]

100%

Lecomte M. C., Nicolas G., Fournier C., Galand C., Malbert-Colas L., Bournier O., Dhermy D., Grandchamp B.

Cellular and Molecular Biology Letters

2001

tom 06

nr 2

Modulatory effect of divalent metal cations on the phosphotyrosine activity of the frog liver acid phosphatase

86%

Szalewicz A., Strzelczyk B., Kubicz A.

Acta Biochimica Polonica

1999

tom 46

nr 1

Frog liver acid phosphatase hydrolyzes phosphotyrosine at acidic pH optimum. Mn2+, Ca2+ and Mg2+ (but not Zn2+) ions modulate this activity by shifting its pH optimum to physiological pH. This effect is not observed when p-nitrophenylphos-phate is used as a substrate. Phosphoserine and phosphothreonine are not hydrolyzed under the same conditions.

Ograniczanie wyników

1 Acta Biochimica Polonica

1 Cellular and Molecular Biology Letters

1 Bournier O.

1 Dhermy D.

1 Fournier C.

1 Galand C.

1 Grandchamp B.

1 Kubicz A.

1 Lecomte M. C.

1 Malbert-Colas L.

1 Nicolas G.

1 Strzelczyk B.

1 Szalewicz A.

1 2001

1 1999

Wyniki wyszukiwania

Interaction of spectrin with the low molecular weight phosphotyrosine phosphatase [LMW-PTP]

Modulatory effect of divalent metal cations on the phosphotyrosine activity of the frog liver acid phosphatase